Journal
SCIENCE
Volume 366, Issue 6461, Pages 100-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aay0967
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Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt) [SPP 2002]
- Japan Society for the Promotion of Science [16K07299]
- University of Strasbourg
- CNRS (France)
- Nobel Laureate Fellowship of the Max Planck Society
- Grants-in-Aid for Scientific Research [16K07299] Funding Source: KAKEN
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Cytochrome bd-type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo-electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily-specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.
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